|Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro.
|Overexpression of Hp95 induces G1 phase arrest in confluent HeLa cells.
|The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting.
|AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding.
|The protein network of HIV budding.
|Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins.
|Structure and function of human Vps20 and Snf7 proteins.
|CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms.
|Complete sequencing and characterization of 21,243 full-length human cDNAs.
|Role of LBPA and Alix in multivesicular liposome formation and endosome organization.
|The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
|Identification of Rab GTPase-activating protein-like protein (RabGAPLP) as a novel Alix/AIP1-interacting protein.
|Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding.
|The DNA sequence, annotation and analysis of human chromosome 3.
|The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A.
|Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.
|Structural basis for viral late-domain binding to Alix.
|Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding.
|Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site.
|Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery.
|Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis.
|Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV.
|Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants.
|ALIX-CHMP4 interactions in the human ESCRT pathway.
|Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release.
|A quantitative atlas of mitotic phosphorylation.
|Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide complex: Ca2+/EF3-driven arginine switch mechanism.
|Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55.
|Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
|Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101.
|Lysine acetylation targets protein complexes and co-regulates major cellular functions.
|Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site.
|Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
|Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration.
|Multiple interactions between the ESCRT machinery and arrestin-related proteins: implications for PPXY-dependent budding.
|Initial characterization of the human central proteome.
|Exome-sequencing confirms DNAJC5 mutations as cause of adult neuronal ceroid-lipofuscinosis.
|Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
|Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.
|Toward a comprehensive characterization of a human cancer cell phosphoproteome.
|Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
|An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
|N-terminome analysis of the human mitochondrial proteome.